Abstract：
:Four proteins were isolated from depectinised elementary fibres of flax (Linum usitatissimum L.), using either alkali or cellulase digestion treatments. All the four proteins were characterized by a deficiency or low contents of hydroxyproline and by high levels of glutamic acid/glutamine and/or aspartic acid/asparagine. The two proteoglycans solubilized with cellulase strongly reacted with beta-glucosyl Yariv reagent but not with alpha-glucosyl Yariv reagent and contained appreciable amounts of alanine, glycine, serine and threonine, suggesting a relationship with cell wall hydroxyproline-deficient arabinogalactan-proteins. The two alkali-extracted proteins did not show any reaction with beta-glucosyl Yariv dye. Due to the harsh treatment, they might only partially represent the original proteins. Due to its high level of glycine (41%), one of these proteins might be classified as a glycine-rich protein. The latter polypeptide, of low molecular molar mass, contained 14.6% leucine and might consist of a domain related to leucine-rich proteins. The data show that these proteins and arabinogalactan-protein-like proteoglycans were strongly associated with the secondary walls of flax fibres. Their presence in small amounts (0.1-0.4%), raises the problem of their putative structural role.
journal_name
Plantajournal_title
Plantaauthors
Girault R,His I,Andeme-Onzighi C,Driouich A,Morvan Cdoi
10.1007/s004250000281subject
Has Abstractpub_date
2000-07-01 00:00:00pages
256-64issue
2eissn
0032-0935issn
1432-2048pii
10.1007/s004250000281journal_volume
211pub_type
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